1obb
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1obb.gif|left|200px]] | [[Image:1obb.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1obb", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | | | + | --> |
| - | | | + | {{STRUCTURE_1obb| PDB=1obb | SCENE= }} |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''ALPHA-GLUCOSIDASE A, AGLA, FROM THERMOTOGA MARITIMA IN COMPLEX WITH MALTOSE AND NAD+''' | '''ALPHA-GLUCOSIDASE A, AGLA, FROM THERMOTOGA MARITIMA IN COMPLEX WITH MALTOSE AND NAD+''' | ||
| Line 31: | Line 28: | ||
[[Category: Maier, T.]] | [[Category: Maier, T.]] | ||
[[Category: Strater, N.]] | [[Category: Strater, N.]] | ||
| - | [[Category: | + | [[Category: Glycosidase]] |
| - | [[Category: | + | [[Category: Hydrolase]] |
| - | [[Category: | + | [[Category: Maltose]] |
| - | [[Category: | + | [[Category: Nad+]] |
| - | [[Category: | + | [[Category: Sulfinic acid]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:37:38 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 00:37, 3 May 2008
ALPHA-GLUCOSIDASE A, AGLA, FROM THERMOTOGA MARITIMA IN COMPLEX WITH MALTOSE AND NAD+
Overview
Glycoside hydrolase family 4 represents an unusual group of glucosidases with a requirement for NAD+, divalent metal cations, and reducing conditions. The family is also unique in its inclusion of both alpha- and beta-specific enzymes. The alpha-glucosidase A, AglA, from Thermotoga maritima is a typical glycoside hydrolase family 4 enzyme, requiring NAD+ and Mn2+ as well as strongly reducing conditions for activity. Here we present the crystal structure of the protein complexed with NAD+ and maltose, refined at a resolution of 1.9 A. The NAD+ is bound to a typical Rossman fold NAD+-binding site, and the nicotinamide moiety is localized close to the maltose substrate. Within the active site the conserved Cys-174 and surrounding histidines are positioned to play a role in the hydrolysis reaction. The electron density maps indicate that Cys-174 is oxidized to a sulfinic acid. Most likely, the strongly reducing conditions are necessary to reduce the oxidized cysteine side chain. Notably, the canonical set of catalytic acidic residues common to other glucosidases is not present in the active site. This, combined with a high structural homology to NAD-dependent dehydrogenases, suggests an unusual and possibly unique mechanism of action for a glycoside-hydrolyzing enzyme.
About this Structure
1OBB is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
Reference
Crystal structure of Thermotoga maritima alpha-glucosidase AglA defines a new clan of NAD+-dependent glycosidases., Lodge JA, Maier T, Liebl W, Hoffmann V, Strater N, J Biol Chem. 2003 May 23;278(21):19151-8. Epub 2003 Feb 14. PMID:12588867 Page seeded by OCA on Sat May 3 03:37:38 2008
